2K4W
The Solution Structure of the Monomeric Copper, Zinc Superoxide Dismutase from Salmonella enterica
Summary for 2K4W
| Entry DOI | 10.2210/pdb2k4w/pdb |
| NMR Information | BMRB: 15112 |
| Descriptor | Superoxide dismutase [Cu-Zn], COPPER (I) ION, ZINC ION (3 entities in total) |
| Functional Keywords | superoxide dismutase, solution structures, metalloenzymes, bioinorganic chemistry, copper, metal-binding, oxidoreductase, zinc, structural genomics, nppsfa, national project on protein structural and functional analyses, structural proteomics in europe, spine |
| Biological source | Salmonella enterica subsp. enterica serovar Choleraesuis |
| Total number of polymer chains | 1 |
| Total formula weight | 15867.62 |
| Authors | Mori, M.,Jimenez, B.,Piccioli, M.,Battistoni, A.,Sette, M.,Structural Proteomics in Europe (SPINE) (deposition date: 2008-06-20, release date: 2008-11-18, Last modification date: 2024-11-27) |
| Primary citation | Mori, M.,Jimenez, B.,Piccioli, M.,Battistoni, A.,Sette, M. The Solution Structure of the Monomeric Copper, Zinc Superoxide Dismutase from Salmonella enterica: Structural Insights To Understand the Evolution toward the Dimeric Structure. Biochemistry, 47:12954-12963, 2008 Cited by PubMed Abstract: The structure of the SodCII-encoded monomeric Cu, Zn superoxide dismutase from Salmonella enterica has been solved by NMR spectroscopy. This represents the first solution structure of a natural and fully active monomeric superoxide dismutase in solution, providing information useful for the interpretation of the evolutional development of these enzymes. The protein scaffold consists of the characteristic beta-barrel common to the whole enzyme family. The general shape of the protein is quite similar to that of Escherichia coli Cu, Zn superoxide dismutase, although some differences are observed mainly in the active site. SodCII presents a more rigid conformation with respect to the engineered monomeric mutants of the human Cu, Zn superoxide dismutase, even though significant disorder is still present in the loops shaping the active site. The analysis of both dynamics and hydration properties of the protein in solution highlights the factors required to maintain the fully active and, at the same time, monomeric protein. This study provides novel insights into the functional differences between monomeric and dimeric bacterial Cu, Zn superoxide dismutases, in turn helping to explain the convergent evolution toward a dimeric structure in prokaryotic and eukaryotic enzymes of this class. PubMed: 19006322DOI: 10.1021/bi801252e PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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